Ask the Users

An end user shares how her company uses mass spectrometry and how she went about selecting the MS systems in her facility in a brief Q&A.

Written byJames Netterwald
| 3 min read
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Our user: Rachel Garlish, Ph.D., Principal Scientist, UCB, Slough, UK

Cartoon ScientistQ: Please tell me how your company uses mass spectrometry.

A: UCB uses mass spectrometry in several different ways. Our lab in the Department of Physical and Analytical Sciences, New Medicines, uses it for a broad range of applications. At the very high end, we use LCMS to perform experiments involving hydrogen deuterium exchange for epitope mapping on proteins. For this application, we use the nanoACQUITY UPLC system and SYNAPT G2 mass spectrometer from Waters Corporation. We have ancillary accessories for this system, including the HDX manager box. The SYNAPT G2 instrument allows us to separate molecules by size and shape as well as by mass with ion mobility MS, and with its associated software we can efficiently analyze the data.

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Q: What caused you to select those particular MS systems for your work?

A: I believe Waters sells the only commercially available instrument that can perform hydrogen deuterium exchange. It is a complete solution for this application. We can use this instrument from the robotic liquid handling right through to data handling. The most important aspects of this mass spectrometer are its robustness and ease of use. The latter is important because we want our scientists to get up and running quickly. There are several things about this instrument that enable it to perform the hydrogen deuterium exchange. The first is definitely the automation, or robotic side, of liquid handling. The nanoACQUITY UPLC allows for very efficient chromatographic separation. Also, all our experiments must be performed at 0°C, so the HDX manager box allows us to cool the sample and do chromatography under those conditions.

“At the very high end, we use LC-MS to perform experiments involving hydrogen deuterium exchange for epitope mapping on proteins.”

 

 

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